View source for 1vd4


==Solution structure of the zinc finger domain of TFIIE alpha==
<StructureSection load='1vd4' size='340' side='right'caption='[[1vd4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vd4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VD4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vd4 OCA], [https://pdbe.org/1vd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vd4 RCSB], [https://www.ebi.ac.uk/pdbsum/1vd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vd4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/T2EA_HUMAN T2EA_HUMAN] Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/1vd4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vd4 ConSurf].
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== Publication Abstract from PubMed ==
The zinc finger domain in the large subunit of TFIIE (TFIIEalpha) is phylogenetically conserved and is essential for transcription. Here, we determined the solution structure of this domain by using NMR. It consisted of one alpha-helix and five beta-strands, showing novel features distinct from previously determined zinc-binding structures. We created point mutants of TFIIEalpha in this domain and examined their binding abilities to other general transcription factors as well as their transcription activities. Four Zn(2+)-ligand mutants, in which each of cysteine residues at positions 129, 132, 154, and 157 was replaced by alanine, possessed no transcription activities on a linearized template, whereas, on a supercoiled template, interesting functional asymmetry was observed: although the C-terminal two mutants abolished transcription activity (&lt;5%), the N-terminal two mutants retained about 20% activities. The N-terminal two mutants bound stronger to the small subunit of TFIIF than the wild type and the C-terminal two mutants were impaired in their binding abilities to the XPB subunits of TFIIH. These suggest that the structural integrity of the zinc finger domain is essential for the TFIIE function, particularly in the transition from the transcription initiation to elongation and the conformational tuning of this domain for appropriate positioning of TFIIF, TFIIH, and polymerase II would be needed depending on the situation and timing.

A novel zinc finger structure in the large subunit of human general transcription factor TFIIE.,Okuda M, Tanaka A, Arai Y, Satoh M, Okamura H, Nagadoi A, Hanaoka F, Ohkuma Y, Nishimura Y J Biol Chem. 2004 Dec 3;279(49):51395-403. Epub 2004 Sep 22. PMID:15385556<ref>PMID:15385556</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1vd4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arai Y]]
[[Category: Hanaoka F]]
[[Category: Nagadoi A]]
[[Category: Nishimura Y]]
[[Category: Ohkuma Y]]
[[Category: Okamura H]]
[[Category: Okuda M]]
[[Category: Satoh M]]
[[Category: Tanaka A]]